7SJ5
Bacteriophage lambda major capsid protein mutant - W308A
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ALS BEAMLINE 4.2.2 |
Synchrotron site | ALS |
Beamline | 4.2.2 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2017-09-30 |
Detector | CUSTOM-MADE |
Wavelength(s) | 1 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 170.153, 95.303, 113.121 |
Unit cell angles | 90.00, 127.92, 90.00 |
Refinement procedure
Resolution | 29.750 - 2.695 |
Rwork | 0.207 |
R-free | 0.22950 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 3bqw |
RMSD bond length | 0.002 |
RMSD bond angle | 0.457 |
Data reduction software | XDS |
Data scaling software | pointless |
Phasing software | PHENIX |
Refinement software | PHENIX (dev-3724) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 29.750 | 2.791 |
High resolution limit [Å] | 2.695 | 2.695 |
Rmerge | 0.056 | |
Rmeas | 0.065 | |
Rpim | 0.034 | |
Number of reflections | 39376 | 3819 |
<I/σ(I)> | 18.27 | |
Completeness [%] | 99.5 | |
Redundancy | 3.7 | |
CC(1/2) | 0.999 | 0.919 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 5.7 | 291.15 | 0.1 M bis-tris, 0.1 M ammonium sulfate, 5% v/v glycerol, 30% v/v PEG-3350 |